The length of peptide substrates has a marked effect on hydroxylation by the hypoxia-inducible factor prolyl 4-hydroxylases.
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Evidence for the slow reaction of hypoxia-inducible factor prolyl hydroxylase 2 with oxygenHypoxia-Inducible Histone Lysine Demethylases: Impact on the Aging Process and Age-Related DiseasesPeptide substrates for Rho-associated kinase 2 (Rho-kinase 2/ROCK2)The putative RNA helicase HELZ promotes cell proliferation, translation initiation and ribosomal protein S6 phosphorylationSubstrate preference of the HIF-prolyl hydroxylase-2 (PHD2) and substrate-induced conformational change.A yeast three-hybrid system that reconstitutes mammalian hypoxia inducible factor regulatory machineryA phylogenetic approach to gene expression data: evidence for the evolutionary origin of mammalian leukocyte phenotypesMyeloid knockout of HIF-1 α does not markedly affect hemorrhage/resuscitation-induced inflammation and hepatic injury.Inhibition of hypoxia-inducible factor-targeting prolyl hydroxylase domain-containing protein 2 (PHD2) enhances matrix synthesis by human chondrocytes.Differential sensitivity of hypoxia inducible factor hydroxylation sites to hypoxia and hydroxylase inhibitorsA genetic mechanism for Tibetan high-altitude adaptation.Spermidine/spermine-N1-acetyltransferase 2 is an essential component of the ubiquitin ligase complex that regulates hypoxia-inducible factor 1alpha.Spermidine/spermine N(1)-acetyltransferase-1 binds to hypoxia-inducible factor-1alpha (HIF-1alpha) and RACK1 and promotes ubiquitination and degradation of HIF-1alpha.Nothing Iffy about HIF in the Hypothalamus.Peroxiredoxin-5 targeted to the mitochondrial intermembrane space attenuates hypoxia-induced reactive oxygen species signallingNon-heme dioxygenases: cellular sensors and regulators jelly rolled into one?Hypoxia inducible factor prolyl 4-hydroxylase enzymes: center stage in the battle against hypoxia, metabolic compromise and oxidative stress.Prolyl 4-hydroxylase activity-responsive transcription factors: from hydroxylation to gene expression and neuroprotection.Turn me on: regulating HIF transcriptional activity.Increased Turnover at Limiting O2 Concentrations by the Thr(387) → Ala Variant of HIF-Prolyl Hydroxylase PHD2.The 2-oxoglutarate analog 3-oxoglutarate decreases normoxic hypoxia-inducible factor-1α in cancer cells, induces cell death, and reduces tumor xenograft growth.Genetic causes of erythrocytosis and the oxygen-sensing pathway.Prolyl hydroxylase 2 deficiency limits proliferation of vascular smooth muscle cells by hypoxia-inducible factor-1{alpha}-dependent mechanisms.Double oxygen-sensing vector system for robust hypoxia/ischemia-regulated gene induction in cardiac muscle in vitro and in vivo.Signaling hypoxia by hypoxia-inducible factor protein hydroxylases: a historical overview and future perspectivesProlyl 4-hydroxylases, key enzymes in the synthesis of collagens and regulation of the response to hypoxia, and their roles as treatment targets.Taking advantage of tumor cell adaptations to hypoxia for developing new tumor markers and treatment strategies.Study on the expressions of PHD and HIF in placentas from normal pregnant women and patients with preeclampsia.HIF and pulmonary vascular responses to hypoxia.Perspective in chronic kidney disease: targeting hypoxia-inducible factor (HIF) as potential therapeutic approach.Oxygen sensing and hypoxia signalling pathways in animals: the implications of physiology for cancer.Prolyl 4-hydroxylases, master regulators of the hypoxia response.Structure-based drug design for hypoxia-inducible factor prolyl-hydroxylase inhibitors and its therapeutic potential for the treatment of erythropoiesis-stimulating agent-resistant anemia: raising expectations for exploratory clinical trials.Non-enzymatic chemistry enables 2-hydroxyglutarate-mediated activation of 2-oxoglutarate oxygenases.Requirements for Skp1 processing by cytosolic prolyl 4(trans)-hydroxylase and α-N-acetylglucosaminyltransferase enzymes involved in O₂ signaling in dictyostelium.Oxygen availability and metabolic adaptations.Transformation by the (R)-enantiomer of 2-hydroxyglutarate linked to EGLN activation.Utilization of an in vivo reporter for high throughput identification of branched small molecule regulators of hypoxic adaptation.Nuclear oxygen sensing: induction of endogenous prolyl-hydroxylase 2 activity by hypoxia and nitric oxide.An endoplasmic reticulum transmembrane prolyl 4-hydroxylase is induced by hypoxia and acts on hypoxia-inducible factor alpha.
P2860
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P2860
The length of peptide substrates has a marked effect on hydroxylation by the hypoxia-inducible factor prolyl 4-hydroxylases.
description
2006 nî lūn-bûn
@nan
2006 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
name
The length of peptide substrat ...... factor prolyl 4-hydroxylases.
@ast
The length of peptide substrat ...... factor prolyl 4-hydroxylases.
@en
The length of peptide substrat ...... factor prolyl 4-hydroxylases.
@nl
type
label
The length of peptide substrat ...... factor prolyl 4-hydroxylases.
@ast
The length of peptide substrat ...... factor prolyl 4-hydroxylases.
@en
The length of peptide substrat ...... factor prolyl 4-hydroxylases.
@nl
prefLabel
The length of peptide substrat ...... factor prolyl 4-hydroxylases.
@ast
The length of peptide substrat ...... factor prolyl 4-hydroxylases.
@en
The length of peptide substrat ...... factor prolyl 4-hydroxylases.
@nl
P2093
P2860
P356
P1476
The length of peptide substrat ...... factor prolyl 4-hydroxylases.
@en
P2093
Johanna Myllyharju
Kari I Kivirikko
Maija Hirsilä
Peppi Koivunen
P2860
P304
28712-28720
P356
10.1074/JBC.M604628200
P407
P577
2006-08-01T00:00:00Z